Autophagy-related protein

spinqualitylabelsall models Yeast Atg7 C terminal (green) complex with Atg8 (magenta) and Zn+2 ion (grey) (PDB code 3vh3) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Autophagy-related proteins (Atg) function in autophagosome formation from the pre-autophagosomal structure (PAS). The phagosomes perform protein degradation under starvation. Autophagy is the process of forming a vacuole around proteins or nucleic acids destined to be broken down. This vacuole is a double membrane enclosure called phagophore. Atgs have non-autophagic functions as well as they are involved in cell survival and apoptosis. So far 34 Atgs have been identified in yeast. Atg1, 6, 14 are involved in the formation of the phagophore. Atg2 is essential for autophagosome formation. Atg3 catalyzes the conjugation of Atg8 and phosphatidylethanolamine. This conjugation is essential for autophagosome formation. Atg4, 5, 7, 10, 16 are involved in the maturation of the phagophore. Atg8 is structurally similar to ubiquitin. It is a targeting factor in cytoplasm-to-vacuole transport of proteins such as aminopeptidase and a-mannosidase. Microtubule-associated protein light chain 3 LC3 is a mammalian Atg8. Atg9 mediates autophagosomal membrane expansion. Atg11 is essential for selective autophagy. Atg12 is involved in the elongation of the phagophore. Atg13, 17 are PAS scaffold proteins. Atg18 forms a complex with Atg2 which tethers membranes to the ER for autophagosome formation. Atg101 is believed to protect Atg13 from proteasomal degradation. Structural highlights Yeast Atg7 C terminal complex with Atg8 and Zn+2 ion (PDB code 3vh3). Zn+2 ion is bound with 4 Cys residues in yeast Atg7 C-terminal domain. 3D Structures of autophagy-related protein Autophagy-related protein 3D structures

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Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman